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Gene Review

Akap12  -  A kinase (PRKA) anchor protein (gravin) 12

Mus musculus

Synonyms: A-kinase anchor protein 12, AI317366, AKAP-12, Gag12, Germ cell lineage protein gercelin, ...
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Disease relevance of Akap12

  • Our data suggest a role for the loss of SSeCKS/Gravin in the metastatic progression of human prostate cancer [1].
  • SSeCKS/Gravin expression was detected in benign human prostatic lesions and well-differentiated carcinomas but not in undifferentiated lesions with Gleason sums > or =6 [1].
  • In nude mice, SSeCKS reexpression slightly decreased primary-site tumor growth but severely decreased the formation of lung metastases [1].

High impact information on Akap12


Biological context of Akap12


Anatomical context of Akap12

  • Short-term addition of phorbol esters caused the movement of SSeCKS from plasma membrane sites to the perinucleus coincident with a loss of actin stress fibers [5].
  • These data suggest that mitogen-induced, FAK-dependent tyrosine phosphorylation of SSeCKS modulates its binding to the actin-based cytoskeleton, suggesting a role for SSeCKS in mitogen-induced cytoskeletal reorganization [9].
  • In this study, we report the generation, via gene trapping in embryonic stem cells of mice carrying an insertion in the mouse SSeCKS gene [6].
  • Finally, we show that P1- but not P2-mRNA expression is abolished by the insertion and furthermore that mice homozygous for the mutation lack SSeCKS in all tissues except the male germ cells [6].
  • Ectopic expression of SSeCKS caused loss of cytoplasmic F-actin fibers in the mouse endothelial cell line LEII [10].

Associations of Akap12 with chemical compounds


Physical interactions of Akap12

  • This correlated with increased coprecipitation of SSeCKS with biotin-phalloidin-bound F-actin from FAK-/- compared to FAK+/+ cell lysates [9].
  • The mitogenic regulatory activity of SSeCKS is likely manifested by its ability to bind key signalling proteins such as protein kinases C and A and calmodulin, and to control actin-based cytoskeletal architecture [11].

Enzymatic interactions of Akap12


Regulatory relationships of Akap12


Other interactions of Akap12


Analytical, diagnostic and therapeutic context of Akap12


  1. The Src-suppressed C kinase substrate, SSeCKS, is a potential metastasis inhibitor in prostate cancer. Xia, W., Unger, P., Miller, L., Nelson, J., Gelman, I.H. Cancer Res. (2001) [Pubmed]
  2. SSeCKS regulates angiogenesis and tight junction formation in blood-brain barrier. Lee, S.W., Kim, W.J., Choi, Y.K., Song, H.S., Son, M.J., Gelman, I.H., Kim, Y.J., Kim, K.W. Nat. Med. (2003) [Pubmed]
  3. SSeCKS, a major protein kinase C substrate with tumor suppressor activity, regulates G(1)-->S progression by controlling the expression and cellular compartmentalization of cyclin D. Lin, X., Nelson, P., Gelman, I.H. Mol. Cell. Biol. (2000) [Pubmed]
  4. v-Jun targets showing an expression pattern that correlates with the transformed cellular phenotype. Iacovoni, J.S., Cohen, S.B., Berg, T., Vogt, P.K. Oncogene (2004) [Pubmed]
  5. A novel src- and ras-suppressed protein kinase C substrate associated with cytoskeletal architecture. Lin, X., Tombler, E., Nelson, P.J., Ross, M., Gelman, I.H. J. Biol. Chem. (1996) [Pubmed]
  6. Gene trap insertion reveals two open reading frames in the mouse SSeCKS gene: the form predominantly detected in the nervous system is suppressed by the insertion while the other, specific of the testis, remains expressed. Camus, A., Mesbah, K., Rallu, M., Babinet, C., Barra, J. Mech. Dev. (2001) [Pubmed]
  7. Control of cytoskeletal architecture by the src-suppressed C kinase substrate, SSeCKS. Gelman, I.H., Lee, K., Tombler, E., Gordon, R., Lin, X. Cell Motil. Cytoskeleton (1998) [Pubmed]
  8. Calmodulin and cyclin D anchoring sites on the Src-suppressed C kinase substrate, SSeCKS. Lin, X., Gelman, I.H. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  9. Mitogen-induced, FAK-dependent tyrosine phosphorylation of the SSeCKS scaffolding protein. Xia, W., Gelman, I.H. Exp. Cell Res. (2002) [Pubmed]
  10. Induction of Src-suppressed C kinase substrate (SSeCKS) in vascular endothelial cells by bacterial lipopolysaccharide. Kitamura, H., Okita, K., Fujikura, D., Mori, K., Iwanaga, T., Saito, M. J. Histochem. Cytochem. (2002) [Pubmed]
  11. A role for SSeCKS, a major protein kinase C substrate with tumour suppressor activity, in cytoskeletal architecture, formation of migratory processes, and cell migration during embryogenesis. Gelman, I.H., Tombler, E., Vargas, J. Histochem. J. (2000) [Pubmed]
  12. Reexpression of the major protein kinase C substrate, SSeCKS, suppresses v-src-induced morphological transformation and tumorigenesis. Lin, X., Gelman, I.H. Cancer Res. (1997) [Pubmed]
  13. SSeCKS/Gravin/AKAP12 attenuates expression of proliferative and angiogenic genes during suppression of v-Src-induced oncogenesis. Liu, Y., Gao, L., Gelman, I.H. BMC Cancer (2006) [Pubmed]
  14. The expression of src-suppressed C kinase substrate (SSeCKS) and uptake of exogenous particles in endothelial and reticular cells. Rung-ruangkijkrai, T., Fujikura, D., Kitamura, H., Saito, M., Iwanaga, T. Arch. Histol. Cytol. (2004) [Pubmed]
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